4UV0

Structure of a semisynthetic phosphorylated DAPK

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PGE A 1303

Chain	Residue
A	ALA40
A	PHE162
A	LYS42
A	GLU64
A	ILE77
A	LEU93
A	GLU94
A	VAL96
A	ILE160
A	ASP161

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAVVKkCrekstglqyaak......FIKK

Chain	Residue	Details
A	LEU19-LYS46

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site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHfDLKpeNIML

Chain	Residue	Details
A	ILE135-LEU147

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP139

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
A	LEU19
A	LYS42
A	GLU94
A	GLU100
A	ASP161

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine; by RPS6KA1 and RPS6KA3 => ECO:0000269|PubMed:16213824

Chain	Residue	Details
A	CYS289

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11579085, ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:17056602

Chain	Residue	Details
A	SER308

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER319

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